ID   KHK_MOUSE               Reviewed;         298 AA.
AC   P97328; Q91WU8;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Ketohexokinase {ECO:0000312|MGI:MGI:1096353};
DE            EC=2.7.1.3 {ECO:0000250|UniProtKB:P50053};
DE   AltName: Full=Hepatic fructokinase;
GN   Name=Khk {ECO:0000312|MGI:MGI:1096353};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hayward B.E., Bonthron D.T.;
RT   "Structure and function of the fructokinase gene.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to
CC       fructose-1-phosphate. {ECO:0000250|UniProtKB:P50053}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose + ATP = beta-D-fructose 1-phosphate + ADP +
CC         H(+); Xref=Rhea:RHEA:18145, ChEBI:CHEBI:15378, ChEBI:CHEBI:28645,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:138881, ChEBI:CHEBI:456216;
CC         EC=2.7.1.3; Evidence={ECO:0000250|UniProtKB:P50053};
CC   -!- ACTIVITY REGULATION: Requires potassium. Inhibition by ADP (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate metabolism; fructose metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50053}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; Y09335; CAA70515.1; -; mRNA.
DR   EMBL; BC013464; AAH13464.1; -; mRNA.
DR   CCDS; CCDS39050.1; -.
DR   RefSeq; NP_032465.2; NM_008439.4.
DR   PDB; 6P2D; X-ray; 1.79 A; A=2-298.
DR   PDB; 8OMD; X-ray; 2.00 A; A/B/C/D=2-298.
DR   PDB; 8OMG; X-ray; 1.82 A; A/B=1-298.
DR   AlphaFoldDB; P97328; -.
DR   SMR; P97328; -.
DR   FunCoup; P97328; 766.
DR   IntAct; P97328; 2.
DR   STRING; 10090.ENSMUSP00000031053; -.
DR   BindingDB; P97328; -.
DR   GlyGen; P97328; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P97328; -.
DR   PhosphoSitePlus; P97328; -.
DR   SwissPalm; P97328; -.
DR   jPOST; P97328; -.
DR   PaxDb; 10090-ENSMUSP00000031053; -.
DR   PeptideAtlas; P97328; -.
DR   ProteomicsDB; 263597; -.
DR   DNASU; 16548; -.
DR   GeneID; 16548; -.
DR   UCSC; uc008wwn.1; mouse.
DR   AGR; MGI:1096353; -.
DR   CTD; 3795; -.
DR   MGI; MGI:1096353; Khk.
DR   eggNOG; KOG2947; Eukaryota.
DR   InParanoid; P97328; -.
DR   OrthoDB; 204058at2759; -.
DR   PhylomeDB; P97328; -.
DR   BRENDA; 2.7.1.3; 3474.
DR   Reactome; R-MMU-70350; Fructose catabolism.
DR   UniPathway; UPA00202; -.
DR   BioGRID-ORCS; 16548; 4 hits in 78 CRISPR screens.
DR   PRO; PR:P97328; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P97328; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:GO_Central.
DR   GO; GO:0070061; F:fructose binding; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0004454; F:ketohexokinase activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central.
DR   GO; GO:0006001; P:fructose catabolic process; IDA:MGI.
DR   GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; IMP:MGI.
DR   GO; GO:0006000; P:fructose metabolic process; IMP:MGI.
DR   GO; GO:0061625; P:glycolytic process through fructose-1-phosphate; IC:MGI.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IMP:MGI.
DR   GO; GO:0070873; P:regulation of glycogen metabolic process; IBA:GO_Central.
DR   GO; GO:0009749; P:response to glucose; ISO:GO_Central.
DR   GO; GO:0032868; P:response to insulin; ISO:GO_Central.
DR   GO; GO:0009744; P:response to sucrose; ISO:GO_Central.
DR   GO; GO:0010043; P:response to zinc ion; ISO:GO_Central.
DR   CDD; cd01939; Ketohexokinase; 1.
DR   FunFam; 3.40.1190.20:FF:000018; Ketohexokinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR052562; Ketohexokinase-related.
DR   InterPro; IPR034093; KHK.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR42774:SF3; KETOHEXOKINASE; 1.
DR   PANTHER; PTHR42774; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PDBsum; 6P2D; -.
DR   PDBsum; 8OMD; -.
DR   PDBsum; 8OMG; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..298
FT                   /note="Ketohexokinase"
FT                   /id="PRO_0000080089"
FT   BINDING         15
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         41
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         42
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         45
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         226..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         255..258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   BINDING         258
FT                   /ligand="beta-D-fructose"
FT                   /ligand_id="ChEBI:CHEBI:28645"
FT                   /evidence="ECO:0000250|UniProtKB:P50053"
FT   CONFLICT        203
FT                   /note="P -> S (in Ref. 2; AAH13464)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          13..22
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:8OMG"
FT   STRAND          33..40
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           42..53
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:8OMG"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           117..121
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           122..126
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          133..142
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           143..158
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          167..172
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           177..184
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          185..191
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           193..198
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           204..211
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           226..228
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          230..233
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          239..242
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           256..269
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           274..288
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:6P2D"
FT   HELIX           295..297
FT                   /evidence="ECO:0007829|PDB:6P2D"
SQ   SEQUENCE   298 AA;  32750 MW;  A8181D781A6136D4 CRC64;
     MEEKQILCVG LVVLDIINVV DKYPEEDTDR RCLSQRWQRG GNASNSCTVL SLLGARCAFM
     GSLAPGHVAD FLVADFRQRG VDVSQVTWQS QGDTPCSCCI VNNSNGSRTI ILYDTNLPDV
     SAKDFEKVDL TRFKWIHIEG RNASEQVKML QRIEEHNAKQ PLPQKVRVSV EIEKPREELF
     QLFSYGEVVF VSKDVAKHLG FQPAVEALRG LYSRVKKGAT LVCAWAEEGA DALGPDGQLL
     HSDAFPPPRV VDTLGAGDTF NASVIFSLSK GNSMQEALRF GCQVAGKKCG LQGFDGIV
//